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Cryo-EM structure of the Ycf2-FtsHi motor complex from Arabidopsis in ATP-bound stateCryo-EM structure of the Ycf2-FtsHi motor complex from Arabidopsis in ATP-bound state
Structural highlights
FunctionFTSI4_ARATH Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis (PubMed:24964212). Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (PubMed:12185496).[1] [2] Publication Abstract from PubMedChloroplast proteins are imported via the translocon at the outer chloroplast membrane (TOC)-translocon at the inner chloroplast membrane (TIC) supercomplex, driven by an ATPase motor. The Ycf2-FtsHi complex has been identified as the chloroplast import motor. However, its assembly and cooperation with the TIC complex during preprotein translocation remain unclear. Here, we present the structures of the Ycf2-FtsHi and TIC complexes from Arabidopsis and an ultracomplex formed between them from Pisum. The Ycf2-FtsHi structure reveals a heterohexameric AAA+ ATPase motor module with characteristic features. Four previously uncharacterized components of Ycf2-FtsHi were identified, which aid in complex assembly and anchoring of the motor module at a tilted angle relative to the membrane. When considering the structures of the TIC complex and the TIC-Ycf2-FtsHi ultracomplex together, it becomes evident that the tilted motor module of Ycf2-FtsHi enables its close contact with the TIC complex, thereby facilitating efficient preprotein translocation. Our study provides valuable structural insights into the chloroplast protein import process in land plants. Structural insights into the chloroplast protein import in land plants.,Liang K, Jin Z, Zhan X, Li Y, Xu Q, Xie Y, Yang Y, Wang S, Wu J, Yan Z Cell. 2024 Aug 21:S0092-8674(24)00894-8. doi: 10.1016/j.cell.2024.08.003. PMID:39197452[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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